Carbon-detected deuterium solid-state NMR rotating frame relaxation measurements for protein methyl groups under magic angle spinning.

ABSTRACT: Deuterium rotating frame solid-state NMR relaxation measurements (²H R_1ρ) are important tools in quantitative studies of molecular dynamics. We demonstrate how ²H to ¹³C cross-polarization (CP) approaches under 10-40 kHz magic angle spinning rates can be combined with the ²H R_1ρ blocks to allow for extension of deuterium rotating frame relaxation studies to methyl groups in biomolecules. This extension permits detection on the ¹³C nuclei and, hence, for the achievement of site-specific resolution. The measurements are demonstrated using a nine-residue low complexity peptide with the sequence GGKGMGFGL, in which a single selective -¹³CD₃ label is placed at the methionine residue. Carbon-detect

SUBMITTER: Vugmeyster L 

PROVIDER: S-EPMC11015826 | biostudies-literature | 2024 Apr

REPOSITORIES: biostudies-literature